Reviewed,
UniProtKB/Swiss-Prot P24815 (3BHS1_MOUSE)
Last modified
June 16, 2009.
Version 74.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1 Short name=3-beta-HSD I Including the following 2 domains: 1- Recommended name: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase EC=1.1.1.145 Alternative name(s): 3-beta-hydroxy-5-ene steroid dehydrogenase Progesterone reductase 2- Recommended name: Steroid Delta-isomerase EC=5.3.3.1 Alternative name(s): Delta-5-3-ketosteroid isomerase | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 373 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. |
| Catalytic activity | A 3-beta-hydroxy-Delta(5)-steroid + NAD+ = a 3-oxo-Delta(5)-steroid + NADH. A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid. |
| Pathway | |
| Subcellular location | Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. |
| Tissue specificity | Steroidogenic tissues (includes testes, ovaries and adrenal glands). |
| Sequence similarities | Belongs to the 3-beta-HSD family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Steroidogenesis |
| Cellular component | Endoplasmic reticulum Membrane Mitochondrion |
| Domain | Transmembrane |
| Ligand | NAD |
| Molecular function | Isomerase Oxidoreductase |
| Technical term | Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | C21-steroid hormone biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW mitochondrial membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 3-beta-hydroxy-delta5-steroid dehydrogenase activity Inferred from electronic annotation. Source: EC bindingInferred from electronic annotation. Source: InterPro steroid delta-isomerase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 373 | 372 | 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1 | PRO_0000087780 | |||||
Regions | |||||||||
| Transmembrane | 288 – 308 | 21 | Potential | ||||||
Sites | |||||||||
| Active site | 155 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 159 | 1 | NAD By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 128 | 1 | V → A in AAH52659. Ref.2 | ||||||
| Sequence conflict | 319 | 1 | L → S in AAH52659. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Multiple forms of mouse 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase and differential expression in gonads, adrenal glands, liver, and kidneys of both sexes." Bain P.A., Yoo M., Clarke T., Hammond S.H., Payne A.H. Proc. Natl. Acad. Sci. U.S.A. 88:8870-8874(1991) [PubMed: 1924345] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: CD-1. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Egg. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| M58567 mRNA. Translation: AAA37860.1. BC052659 mRNA. Translation: AAH52659.1. | |
| IPI | IPI00229070. |
| PIR | I49762. |
| RefSeq | NP_032319.1. |
| UniGene | Mm.140811 |
3D structure databases | |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P24815. |
Genome annotation databases | |
| Ensembl | ENSMUSG00000027871. Mus musculus. [Contig view] |
| GeneID | 15492. |
| KEGG | mmu:15492. |
Organism-specific databases | |
| MGI | MGI:96233. Hsd3b1. |
Phylogenomic databases | |
| HOVERGEN | P24815. |
| OMA | P24815. LQDPKKA. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.145. 244. 5.3.3.1. 244. |
Gene expression databases | |
| ArrayExpress | P24815. |
| Bgee | P24815. |
| GermOnline | ENSMUSG00000027871. Mus musculus. |
Family and domain databases | |
| InterPro | IPR002225. 3Beta_OHSteriod_DH/Estase. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF01073. 3Beta_HSD. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 288366. |
| SOURCE | Search... |
Entry information
| Entry name | 3BHS1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P24815 Secondary accession number(s): Q7TQ00 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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